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Protein Science, Vol 7, Issue 3 580-586, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

Crystallization of phycoerythrin 545 of Rhodomonas lens using detergents and unusual additives

M. BECKER, M. T. STUBBS and R. HUBER
Abteilung fur Strukturforschung, Max-Planck-Institut fur Biochemie, 82152 Martinsried, Germany

Phycoerythrin 545 from the cryptomonad alga, Rhodomonas lens, has been crystallized under a wide variety of conditions. Although this type of photosynthetic light-harvesting protein is water soluble, detergents were always required for crystallization. The crystals were typically poorly ordered, or ordered in only two dimensions. However, crystals that were well-ordered in three dimensions could be obtained under two different conditions. Both used polyethylene glycol as precipitant and the detergent lauryldimethylaminoxide, but the additives that were critical for obtaining well-ordered crystals were propionamide in one case and Cs(+)/Br(-) in the other. Crystals obtained in the presence of propionamide have the space group P2(1)2(1)2(1), with cell constants of a = 85.6 A, b = 108.2 A, and c = 131.0 A, and contain two dimers [i.e., 2 X ({alpha}(2){beta}(2))] in the asymmetric unit. They show diffraction to at least 3.0 A resolution. The crystals grown with Cs(+)/Br(-) are nearly isomorphous. Both types of crystals show intense, strongly polarized fluorescence, suggesting that energy transfer in the crystals is highly efficient. This should provide a basis for quantitative investigation of the role of exciton interactions in energy transfer in cryptomonad phycobiliproteins.
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 Proc. Natl. Acad. Sci. USAHome page
K. E. Wilk, S. J. Harrop, L. Jankova, D. Edler, G. Keenan, F. Sharples, R. G. Hiller, and P. M. G. Curmi
Evolution of a light-harvesting protein by addition of new subunits and rearrangement of conserved elements: Crystal structure of a cryptophyte phycoerythrin at 1.63-A resolution
PNAS, August 3, 1999; 96(16): 8901 - 8906.
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